Table 1.
Data collection and refinement statistics (molecular replacement)
| Crystal 1 | |
|---|---|
| Data collection | |
| Space group | P21 |
| Cell dimensions | |
| a, b, c (Å) | 30.32, 64.41, 38.39 |
| α, β, γ (°) | 90.00, 108.9, 90.00 |
| Resolution (Å) | 30–1.6 (1.66–1.60) |
| R pim | 0.028 (0.163) |
| I / σI | 21.2 (3.2) |
| Completeness (%) | 91.5 (60.6) |
| Redundancy | 2.7 (1.8) |
| Refinement | |
| Resolution (Å) | 30–1.6 |
| No. reflections | 16762 |
| Rwork / Rfree | 0.173/ 0.211 |
| No. atoms | 1468 |
| Protein | 1328 |
| Ligand/ion | 0 |
| Water | 140 |
| B-factors | 20.0 |
| Protein | 19.5 |
| Ligand/ion | N/A |
| Water | 29.6 |
| R.m.s. deviations | |
| Bond lengths (Å) | 0.007 |
| Bond angles (°) | 0.863 |
Diffraction data collected from a single crystal. Values in parentheses are for highest-resolution shell